NP_034860.2
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Related Accession #
Molecular Weight
40.6 kDa
NCBI Official Full Name
annexin A1
NCBI Official Synonym Full Names
annexin A1
NCBI Official Synonym Symbols
Lpc1; Anx-1; Lpc-1; Anx-A1; C430014K04Rik [Similar Products]
NCBI Protein Information
annexin A1
UniProt Protein Name
Annexin A1
UniProt Synonym Protein Names
Annexin I; Annexin-1; Calpactin II; Calpactin-2; Chromobindin-9; Lipocortin I
UniProt Synonym Gene Names
UniProt Entry Name
ANXA1_MOUSE
UniProt Comments for Anxa1
ANXA1: a calcium/phospholipid-binding protein with which promotes membrane fusion and is involved in endocytosis. Has anti-inflammatory properties and inhibits phospholipase A2 activity. Accumulates on internalized vesicles after EGF-stimulated endocytosis, suggesting that it may be required for a late stage in inward vesiculation. Phosphorylated by PKC, EGFR and Chak1. Phosphorylation results in loss of the inhibitory activity. Annexins are a family of structurally related proteins whose common property is calcium-dependent binding to phospholipids. There are at least ten different annexins in mammalian species. Annexins do not contain signal peptides, yet some annexins (A1, A2 and A5) appear to be secreted in a physiologically regulated fashion.
Protein type: Calcium-binding; Lipid-binding
Cellular Component: apical plasma membrane; cell projection; cell surface; cilium; cornified envelope; cytoplasm; cytoplasmic vesicle; endosome; extracellular region; extracellular space; extrinsic to external side of plasma membrane; extrinsic to membrane; focal adhesion; lateral plasma membrane; mast cell granule; membrane; mitochondrial membrane; nucleoplasm; nucleus; plasma membrane; protein complex; sarcolemma; vesicle
Molecular Function: calcium ion binding; calcium-dependent phospholipid binding; calcium-dependent protein binding; double-stranded DNA-dependent ATPase activity; helicase activity; metal ion binding; phospholipase A2 inhibitor activity; phospholipase inhibitor activity; phospholipid binding; protein binding; protein binding, bridging; protein homodimerization activity; single-stranded DNA binding; single-stranded RNA binding; structural molecule activity
Biological Process: actin cytoskeleton reorganization; adaptive immune response; alpha-beta T cell differentiation; arachidonic acid secretion; cell surface receptor linked signal transduction; DNA duplex unwinding; DNA strand renaturation; G-protein signaling, coupled to cyclic nucleotide second messenger; immune system process; inflammatory response; innate immune response; insulin secretion; keratinocyte differentiation; monocyte chemotaxis; myoblast migration involved in skeletal muscle regeneration; negative regulation of exocytosis; negative regulation of protein secretion; negative regulation of T-helper 2 cell differentiation; neutrophil homeostasis; peptide cross-linking; phagocytosis; positive regulation of apoptosis; positive regulation of interleukin-2 production; positive regulation of neutrophil apoptosis; positive regulation of prostaglandin biosynthetic process; positive regulation of T cell proliferation; positive regulation of T-helper 1 cell differentiation; positive regulation of vesicle fusion; regulation of cell proliferation; regulation of cell shape; regulation of hormone secretion; regulation of inflammatory response; regulation of interleukin-1 production; regulation of leukocyte migration; signal transduction
Product References and Citations for Anxa1 recombinant protein
Mouse lipocortin I cDNA.Sakata T., Iwagami S., Tsuruta Y., Suzuki R., Hojo K., Sato K., Teraoka H.Nucleic Acids Res. 16:11818-11818(1988)
Mouse lipocortin I gene structure and chromosomal assignment
gene duplication and the origins of a gene family.Horlick K.R., Cheng I.C., Wong W.T., Wakeland E.K., Nick H.S.Genomics 10:365-374(1991)
cDNA-cloning, sequencing and expression in glucocorticoid-stimulated quiescent Swiss 3T3 fibroblasts of mouse lipocortin I.Philipps C., Rose-John S., Rincke G., Fuerstenberger G., Marks F.Biochem. Biophys. Res. Commun. 159:155-162(1989)
Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing.Lennon N.J., Kho A., Bacskai B.J., Perlmutter S.L., Hyman B.T., Brown R.H. Jr.J. Biol. Chem. 278:50466-50473(2003)
Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry.Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.Mol. Cell. Proteomics 8:904-912(2009)
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.Mol. Cell 50:919-930(2013)
Research Articles on Anxa1
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Products associated with Anxa1 recombinant protein
Pathways associated with Anxa1 recombinant protein
Diseases associated with Anxa1 recombinant protein
Organs/Tissues associated with Anxa1 recombinant protein
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